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Database: PDB
Entry: 6NDE
LinkDB: 6NDE
Original site: 6NDE 
HEADER    CELL ADHESION/TOXIN                     13-DEC-18   6NDE              
TITLE     RHODOCETIN IN COMPLEX WITH THE INTEGRIN ALPHA2-A DOMAIN WITH          
TITLE    2 PRASEDYMIUM                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SNACLEC RHODOCETIN SUBUNIT GAMMA;                          
COMPND   3 CHAIN: A, D, G, J, M, P;                                             
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: SNACLEC RHODOCETIN SUBUNIT DELTA;                          
COMPND   6 CHAIN: B, E, H, K, N, Q;                                             
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: INTEGRIN ALPHA-2;                                          
COMPND   9 CHAIN: C, F, I, L, O, R;                                             
COMPND  10 SYNONYM: CD49 ANTIGEN-LIKE FAMILY MEMBER B,COLLAGEN RECEPTOR,PLATELET
COMPND  11 MEMBRANE GLYCOPROTEIN IA,GPIA,VLA-2 SUBUNIT ALPHA;                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CALLOSELASMA RHODOSTOMA;                        
SOURCE   3 ORGANISM_COMMON: MALAYAN PIT VIPER;                                  
SOURCE   4 ORGANISM_TAXID: 8717;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: CALLOSELASMA RHODOSTOMA;                        
SOURCE   7 ORGANISM_COMMON: MALAYAN PIT VIPER;                                  
SOURCE   8 ORGANISM_TAXID: 8717;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: ITGA2, CD49B;                                                  
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    C-TYPE LECTIN, INTEGRIN, VENOM, COAGULATION, CELL ADHESION, CELL      
KEYWDS   2 ADHESION-TOXIN COMPLEX                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.STETEFELD,M.D.MCDOUGALL,P.C.LOEWEN                                  
REVDAT   1   23-JAN-19 6NDE    0                                                
JRNL        AUTH   J.STETEFELD,M.D.MCDOUGALL,P.C.LOEWEN                         
JRNL        TITL   RHODOCETIN IN COMPLEX WITH THE INTEGRIN ALPHA2-A DOMAIN WITH 
JRNL        TITL 2 PRASEDYMIUM BOUND                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50794                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.294                           
REMARK   3   R VALUE            (WORKING SET) : 0.290                           
REMARK   3   FREE R VALUE                     : 0.369                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2746                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 21486                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 97                                      
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 116.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : 0.17000                                              
REMARK   3    B33 (A**2) : -0.35000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.863         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.745         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 54.970        
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MOLECULAR REPLACEMENT                     
REMARK   4                                                                      
REMARK   4 6NDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000238574.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54903                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 132.351                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.47800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC 5.8.0238                                       
REMARK 200 STARTING MODEL: 5THP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 2.65 M AMMONIUM SULPHATE,    
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      127.12200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       63.56100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      190.68300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     CYS A   135                                                      
REMARK 465     TYR B   123                                                      
REMARK 465     SER B   124                                                      
REMARK 465     MET C   150                                                      
REMARK 465     GLY C   151                                                      
REMARK 465     SER C   152                                                      
REMARK 465     SER C   153                                                      
REMARK 465     HIS C   154                                                      
REMARK 465     HIS C   155                                                      
REMARK 465     HIS C   156                                                      
REMARK 465     HIS C   157                                                      
REMARK 465     HIS C   158                                                      
REMARK 465     HIS C   159                                                      
REMARK 465     SER C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     GLY C   162                                                      
REMARK 465     LEU C   163                                                      
REMARK 465     VAL C   164                                                      
REMARK 465     PRO C   165                                                      
REMARK 465     ARG C   166                                                      
REMARK 465     GLY C   167                                                      
REMARK 465     GLY C   168                                                      
REMARK 465     SER C   169                                                      
REMARK 465     PRO C   170                                                      
REMARK 465     SER C   171                                                      
REMARK 465     SER C   363                                                      
REMARK 465     ILE C   364                                                      
REMARK 465     GLU C   365                                                      
REMARK 465     GLY C   366                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     PHE D     2                                                      
REMARK 465     GLU D   134                                                      
REMARK 465     CYS D   135                                                      
REMARK 465     TYR E   123                                                      
REMARK 465     SER E   124                                                      
REMARK 465     MET F   150                                                      
REMARK 465     GLY F   151                                                      
REMARK 465     SER F   152                                                      
REMARK 465     SER F   153                                                      
REMARK 465     HIS F   154                                                      
REMARK 465     HIS F   155                                                      
REMARK 465     HIS F   156                                                      
REMARK 465     HIS F   157                                                      
REMARK 465     HIS F   158                                                      
REMARK 465     HIS F   159                                                      
REMARK 465     SER F   160                                                      
REMARK 465     SER F   161                                                      
REMARK 465     GLY F   162                                                      
REMARK 465     LEU F   163                                                      
REMARK 465     VAL F   164                                                      
REMARK 465     PRO F   165                                                      
REMARK 465     ARG F   166                                                      
REMARK 465     GLY F   167                                                      
REMARK 465     GLY F   168                                                      
REMARK 465     SER F   169                                                      
REMARK 465     PRO F   170                                                      
REMARK 465     SER F   171                                                      
REMARK 465     SER F   363                                                      
REMARK 465     ILE F   364                                                      
REMARK 465     GLU F   365                                                      
REMARK 465     GLY F   366                                                      
REMARK 465     ASP G     1                                                      
REMARK 465     PHE G     2                                                      
REMARK 465     GLU G   134                                                      
REMARK 465     CYS G   135                                                      
REMARK 465     TYR H   123                                                      
REMARK 465     SER H   124                                                      
REMARK 465     MET I   150                                                      
REMARK 465     GLY I   151                                                      
REMARK 465     SER I   152                                                      
REMARK 465     SER I   153                                                      
REMARK 465     HIS I   154                                                      
REMARK 465     HIS I   155                                                      
REMARK 465     HIS I   156                                                      
REMARK 465     HIS I   157                                                      
REMARK 465     HIS I   158                                                      
REMARK 465     HIS I   159                                                      
REMARK 465     SER I   160                                                      
REMARK 465     SER I   161                                                      
REMARK 465     GLY I   162                                                      
REMARK 465     LEU I   163                                                      
REMARK 465     VAL I   164                                                      
REMARK 465     PRO I   165                                                      
REMARK 465     ARG I   166                                                      
REMARK 465     GLY I   167                                                      
REMARK 465     GLY I   168                                                      
REMARK 465     SER I   169                                                      
REMARK 465     PRO I   170                                                      
REMARK 465     SER I   171                                                      
REMARK 465     SER I   363                                                      
REMARK 465     ILE I   364                                                      
REMARK 465     GLU I   365                                                      
REMARK 465     GLY I   366                                                      
REMARK 465     ASP J     1                                                      
REMARK 465     PHE J     2                                                      
REMARK 465     GLU J   134                                                      
REMARK 465     CYS J   135                                                      
REMARK 465     TYR K   123                                                      
REMARK 465     SER K   124                                                      
REMARK 465     MET L   150                                                      
REMARK 465     GLY L   151                                                      
REMARK 465     SER L   152                                                      
REMARK 465     SER L   153                                                      
REMARK 465     HIS L   154                                                      
REMARK 465     HIS L   155                                                      
REMARK 465     HIS L   156                                                      
REMARK 465     HIS L   157                                                      
REMARK 465     HIS L   158                                                      
REMARK 465     HIS L   159                                                      
REMARK 465     SER L   160                                                      
REMARK 465     SER L   161                                                      
REMARK 465     GLY L   162                                                      
REMARK 465     LEU L   163                                                      
REMARK 465     VAL L   164                                                      
REMARK 465     PRO L   165                                                      
REMARK 465     ARG L   166                                                      
REMARK 465     GLY L   167                                                      
REMARK 465     GLY L   168                                                      
REMARK 465     SER L   169                                                      
REMARK 465     PRO L   170                                                      
REMARK 465     SER L   171                                                      
REMARK 465     SER L   363                                                      
REMARK 465     ILE L   364                                                      
REMARK 465     GLU L   365                                                      
REMARK 465     GLY L   366                                                      
REMARK 465     ASP M     1                                                      
REMARK 465     PHE M     2                                                      
REMARK 465     GLU M   134                                                      
REMARK 465     CYS M   135                                                      
REMARK 465     TYR N   123                                                      
REMARK 465     SER N   124                                                      
REMARK 465     MET O   150                                                      
REMARK 465     GLY O   151                                                      
REMARK 465     SER O   152                                                      
REMARK 465     SER O   153                                                      
REMARK 465     HIS O   154                                                      
REMARK 465     HIS O   155                                                      
REMARK 465     HIS O   156                                                      
REMARK 465     HIS O   157                                                      
REMARK 465     HIS O   158                                                      
REMARK 465     HIS O   159                                                      
REMARK 465     SER O   160                                                      
REMARK 465     SER O   161                                                      
REMARK 465     GLY O   162                                                      
REMARK 465     LEU O   163                                                      
REMARK 465     VAL O   164                                                      
REMARK 465     PRO O   165                                                      
REMARK 465     ARG O   166                                                      
REMARK 465     GLY O   167                                                      
REMARK 465     GLY O   168                                                      
REMARK 465     SER O   169                                                      
REMARK 465     PRO O   170                                                      
REMARK 465     SER O   171                                                      
REMARK 465     SER O   363                                                      
REMARK 465     ILE O   364                                                      
REMARK 465     GLU O   365                                                      
REMARK 465     GLY O   366                                                      
REMARK 465     ASP P     1                                                      
REMARK 465     PHE P     2                                                      
REMARK 465     GLU P   134                                                      
REMARK 465     CYS P   135                                                      
REMARK 465     TYR Q   123                                                      
REMARK 465     SER Q   124                                                      
REMARK 465     MET R   150                                                      
REMARK 465     GLY R   151                                                      
REMARK 465     SER R   152                                                      
REMARK 465     SER R   153                                                      
REMARK 465     HIS R   154                                                      
REMARK 465     HIS R   155                                                      
REMARK 465     HIS R   156                                                      
REMARK 465     HIS R   157                                                      
REMARK 465     HIS R   158                                                      
REMARK 465     HIS R   159                                                      
REMARK 465     SER R   160                                                      
REMARK 465     SER R   161                                                      
REMARK 465     GLY R   162                                                      
REMARK 465     LEU R   163                                                      
REMARK 465     VAL R   164                                                      
REMARK 465     PRO R   165                                                      
REMARK 465     ARG R   166                                                      
REMARK 465     GLY R   167                                                      
REMARK 465     GLY R   168                                                      
REMARK 465     SER R   169                                                      
REMARK 465     PRO R   170                                                      
REMARK 465     SER R   171                                                      
REMARK 465     SER R   363                                                      
REMARK 465     ILE R   364                                                      
REMARK 465     GLU R   365                                                      
REMARK 465     GLY R   366                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER R   184    PR     PR R   401              1.98            
REMARK 500   OD2  ASP P    74     O    LYS Q    75              2.03            
REMARK 500   O    GLN P    79     OG   SER P   101              2.04            
REMARK 500   O    GLN M    79     OG   SER M   101              2.04            
REMARK 500   OH   TYR M    93     OE2  GLU N    47              2.09            
REMARK 500   OD2  ASP M    74     O    LYS N    75              2.11            
REMARK 500   OH   TYR P    93     OE2  GLU Q    47              2.14            
REMARK 500   O    LEU F   312     ND2  ASN F   316              2.14            
REMARK 500   OG   SER A    86     OE2  GLU B    26              2.16            
REMARK 500   O    LEU I   312     ND2  ASN I   316              2.17            
REMARK 500   OG   SER F   286     OE2  GLU F   328              2.18            
REMARK 500   O    ARG D    30     OG1  THR D    33              2.18            
REMARK 500   OE2  GLU P    29     OG   SER Q    79              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER C 184   O   -  C   -  N   ANGL. DEV. =  12.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  12     -123.56     44.78                                   
REMARK 500    GLU A  21      104.55    -49.65                                   
REMARK 500    THR A  24      160.89    -48.53                                   
REMARK 500    ALA A  36      158.13    175.45                                   
REMARK 500    ARG A  76      158.73    -42.85                                   
REMARK 500    SER A  88      -18.36    113.79                                   
REMARK 500    ALA A  89      129.12    -26.80                                   
REMARK 500    ASN A  95       57.77   -148.52                                   
REMARK 500    ASN A  97      151.03    -42.80                                   
REMARK 500    ASP A 120      113.96    -39.44                                   
REMARK 500    PRO B   2      157.67    -43.30                                   
REMARK 500    TYR B   8      117.44   -170.52                                   
REMARK 500    HIS B  33      148.95    149.41                                   
REMARK 500    ASN B  69       83.25     64.02                                   
REMARK 500    LEU B  84       76.60   -102.04                                   
REMARK 500    VAL B  88       20.28   -150.60                                   
REMARK 500    ASP C 203       72.91   -112.65                                   
REMARK 500    LYS C 208     -115.37   -148.10                                   
REMARK 500    ALA C 217     -106.29   -143.34                                   
REMARK 500    ASN C 251       69.34   -100.27                                   
REMARK 500    SER C 290       -1.48    -59.58                                   
REMARK 500    ALA C 319       54.34     34.74                                   
REMARK 500    ASP D  12     -117.58     67.74                                   
REMARK 500    ALA D  36      146.17    177.58                                   
REMARK 500    ARG D  76      165.73    -48.84                                   
REMARK 500    GLU D  78     -170.03    -64.00                                   
REMARK 500    SER D  88      -10.80     87.68                                   
REMARK 500    PHE D 113       34.70     72.62                                   
REMARK 500    TYR D 118      166.32    -46.30                                   
REMARK 500    ASP D 120      105.65    -58.16                                   
REMARK 500    PRO D 132     -144.36    -84.50                                   
REMARK 500    PRO E   2      160.48    -40.88                                   
REMARK 500    HIS E   4      -17.51     89.62                                   
REMARK 500    TYR E   8      120.17   -171.17                                   
REMARK 500    GLU E  18      135.26    -38.66                                   
REMARK 500    THR E  21     -179.79    -64.06                                   
REMARK 500    GLU E  26      -74.94    -39.30                                   
REMARK 500    ALA E  31       38.99    -91.65                                   
REMARK 500    HIS E  33      145.98   -177.15                                   
REMARK 500    TRP E  64      154.99    -48.89                                   
REMARK 500    ASN E  69       81.47     39.04                                   
REMARK 500    PRO E  70       -9.15    -56.93                                   
REMARK 500    ASP E  80        2.00    -67.48                                   
REMARK 500    LYS E  83      136.41    -32.28                                   
REMARK 500    LEU E  84       48.70    -99.86                                   
REMARK 500    VAL E  88       29.01   -144.76                                   
REMARK 500    ASP F 203       78.43   -111.68                                   
REMARK 500    LYS F 208     -120.35   -133.95                                   
REMARK 500    ALA F 217      -96.08   -146.25                                   
REMARK 500    ASN F 251       55.09   -111.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     167 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS B    4     TRP B    5                  138.25                    
REMARK 500 PRO D  132     SER D  133                  148.13                    
REMARK 500 TRP E   89     LEU E   90                 -148.25                    
REMARK 500 PRO G  132     SER G  133                  147.71                    
REMARK 500 TRP H   89     LEU H   90                 -147.10                    
REMARK 500 ALA M   10     TYR M   11                  149.33                    
REMARK 500 TRP N   89     LEU N   90                 -149.01                    
REMARK 500 TRP Q   89     LEU Q   90                 -148.18                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR C 401  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C 182   OG                                                     
REMARK 620 2 SER C 184   OG   74.5                                              
REMARK 620 3 ASP C 283   OD1  83.3  92.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR F 401  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 182   OG                                                     
REMARK 620 2 SER F 184   OG   86.2                                              
REMARK 620 3 ASP F 283   OD1 101.6  93.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 184   OG                                                     
REMARK 620 2 SO4 E 203   O3   75.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR I 401  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER I 182   OG                                                     
REMARK 620 2 SER I 184   OG   87.2                                              
REMARK 620 3 ASP I 283   OD1 109.6  98.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA I 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER I 184   OG                                                     
REMARK 620 2 SO4 H 202   O3   74.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR L 401  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER L 182   OG                                                     
REMARK 620 2 SER L 184   OG   73.3                                              
REMARK 620 3 ASP L 283   OD1  83.8  87.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR O 401  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER O 182   OG                                                     
REMARK 620 2 SER O 184   OG   77.9                                              
REMARK 620 3 ASP O 283   OD1  87.3 100.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PR R 401  PR                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER R 182   OG                                                     
REMARK 620 2 ASP R 283   OD1  86.6                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PR C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PR F 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA F 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PR I 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA I 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL J 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 K 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PR L 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA L 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL M 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 N 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PR O 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA O 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 O 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 Q 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 Q 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PR R 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 R 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA R 404                  
DBREF  6NDE A    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  6NDE B    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  6NDE C  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  6NDE D    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  6NDE E    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  6NDE F  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  6NDE G    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  6NDE H    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  6NDE I  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  6NDE J    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  6NDE K    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  6NDE L  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  6NDE M    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  6NDE N    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  6NDE O  170   366  UNP    P17301   ITA2_HUMAN     170    366             
DBREF  6NDE P    1   135  UNP    D2YW39   SLEC_CALRH       1    135             
DBREF  6NDE Q    1   124  UNP    D2YW40   SLED_CALRH       1    124             
DBREF  6NDE R  170   366  UNP    P17301   ITA2_HUMAN     170    366             
SEQADV 6NDE MET C  150  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY C  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER C  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER C  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS C  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS C  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS C  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS C  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS C  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS C  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER C  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER C  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY C  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE LEU C  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE VAL C  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE PRO C  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE ARG C  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY C  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY C  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER C  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE MET F  150  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY F  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER F  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER F  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS F  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS F  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS F  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS F  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS F  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS F  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER F  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER F  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY F  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE LEU F  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE VAL F  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE PRO F  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE ARG F  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY F  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY F  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER F  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE MET I  150  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY I  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER I  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER I  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS I  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS I  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS I  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS I  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS I  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS I  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER I  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER I  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY I  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE LEU I  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE VAL I  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE PRO I  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE ARG I  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY I  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY I  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER I  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE MET L  150  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY L  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER L  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER L  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS L  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS L  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS L  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS L  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS L  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS L  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER L  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER L  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY L  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE LEU L  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE VAL L  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE PRO L  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE ARG L  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY L  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY L  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER L  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE MET O  150  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY O  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER O  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER O  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS O  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS O  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS O  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS O  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS O  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS O  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER O  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER O  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY O  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE LEU O  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE VAL O  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE PRO O  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE ARG O  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY O  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY O  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER O  169  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE MET R  150  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY R  151  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER R  152  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER R  153  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS R  154  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS R  155  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS R  156  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS R  157  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS R  158  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE HIS R  159  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER R  160  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER R  161  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY R  162  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE LEU R  163  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE VAL R  164  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE PRO R  165  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE ARG R  166  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY R  167  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE GLY R  168  UNP  P17301              EXPRESSION TAG                 
SEQADV 6NDE SER R  169  UNP  P17301              EXPRESSION TAG                 
SEQRES   1 A  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 A  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 A  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 A  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 A  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 A  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 A  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 A  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 A  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 A  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 A  135  PHE PRO SER GLU CYS                                          
SEQRES   1 B  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 B  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 B  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 B  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 B  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 B  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 B  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 B  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 B  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 B  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 C  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 C  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 C  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 C  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 C  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 C  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 C  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 C  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 C  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 C  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 C  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 C  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 C  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 C  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 C  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 C  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 D  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 D  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 D  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 D  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 D  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 D  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 D  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 D  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 D  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 D  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 D  135  PHE PRO SER GLU CYS                                          
SEQRES   1 E  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 E  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 E  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 E  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 E  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 E  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 E  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 E  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 E  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 E  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 F  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 F  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 F  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 F  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 F  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 F  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 F  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 F  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 F  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 F  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 F  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 F  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 F  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 F  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 F  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 F  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 F  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 G  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 G  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 G  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 G  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 G  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 G  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 G  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 G  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 G  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 G  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 G  135  PHE PRO SER GLU CYS                                          
SEQRES   1 H  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 H  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 H  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 H  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 H  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 H  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 H  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 H  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 H  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 H  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 I  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 I  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 I  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 I  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 I  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 I  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 I  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 I  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 I  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 I  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 I  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 I  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 I  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 I  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 I  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 I  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 I  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 J  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 J  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 J  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 J  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 J  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 J  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 J  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 J  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 J  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 J  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 J  135  PHE PRO SER GLU CYS                                          
SEQRES   1 K  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 K  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 K  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 K  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 K  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 K  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 K  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 K  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 K  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 K  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 L  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 L  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 L  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 L  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 L  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 L  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 L  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 L  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 L  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 L  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 L  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 L  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 L  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 L  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 L  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 L  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 L  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 M  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 M  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 M  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 M  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 M  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 M  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 M  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 M  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 M  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 M  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 M  135  PHE PRO SER GLU CYS                                          
SEQRES   1 N  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 N  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 N  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 N  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 N  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 N  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 N  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 N  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 N  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 N  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 O  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 O  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 O  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 O  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 O  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 O  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 O  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 O  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 O  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 O  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 O  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 O  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 O  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 O  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 O  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 O  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 O  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
SEQRES   1 P  135  ASP PHE ASN CYS LEU PRO GLY TRP SER ALA TYR ASP GLN          
SEQRES   2 P  135  HIS CYS TYR GLN ALA PHE ASN GLU PRO LYS THR TRP ASP          
SEQRES   3 P  135  GLU ALA GLU ARG PHE CYS THR GLU GLN ALA LYS ARG GLY          
SEQRES   4 P  135  HIS LEU VAL SER ILE GLY SER ASP GLY GLU ALA ASP PHE          
SEQRES   5 P  135  VAL ALA GLN LEU VAL THR ASN ASN ILE LYS ARG PRO GLU          
SEQRES   6 P  135  LEU TYR VAL TRP ILE GLY LEU ARG ASP ARG ARG LYS GLU          
SEQRES   7 P  135  GLN GLN CYS SER SER GLU TRP SER MET SER ALA SER ILE          
SEQRES   8 P  135  ILE TYR VAL ASN TRP ASN THR GLY GLU SER GLN MET CYS          
SEQRES   9 P  135  GLN GLY LEU ALA ARG TRP THR GLY PHE ARG LYS TRP ASP          
SEQRES  10 P  135  TYR SER ASP CYS GLN ALA LYS ASN PRO PHE VAL CYS LYS          
SEQRES  11 P  135  PHE PRO SER GLU CYS                                          
SEQRES   1 Q  124  CYS PRO LEU HIS TRP SER SER TYR ASN GLY TYR CYS TYR          
SEQRES   2 Q  124  ARG VAL PHE SER GLU LEU LYS THR TRP GLU ASP ALA GLU          
SEQRES   3 Q  124  SER PHE CYS TYR ALA GLN HIS LYS GLY SER ARG LEU ALA          
SEQRES   4 Q  124  SER ILE HIS SER ARG GLU GLU GLU ALA PHE VAL GLY LYS          
SEQRES   5 Q  124  LEU ALA SER GLN THR LEU LYS TYR THR SER MET TRP LEU          
SEQRES   6 Q  124  GLY LEU ASN ASN PRO TRP LYS GLU CYS LYS TRP GLU TRP          
SEQRES   7 Q  124  SER ASP ASP ALA LYS LEU ASP TYR LYS VAL TRP LEU ARG          
SEQRES   8 Q  124  ARG PRO TYR CYS ALA VAL MET VAL VAL LYS THR ASP ARG          
SEQRES   9 Q  124  ILE PHE TRP PHE ASN ARG GLY CYS GLU LYS THR VAL SER          
SEQRES  10 Q  124  PHE VAL CYS LYS PHE TYR SER                                  
SEQRES   1 R  217  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 R  217  LEU VAL PRO ARG GLY GLY SER PRO SER LEU ILE ASP VAL          
SEQRES   3 R  217  VAL VAL VAL CYS ASP GLU SER ASN SER ILE TYR PRO TRP          
SEQRES   4 R  217  ASP ALA VAL LYS ASN PHE LEU GLU LYS PHE VAL GLN GLY          
SEQRES   5 R  217  LEU ASP ILE GLY PRO THR LYS THR GLN VAL GLY LEU ILE          
SEQRES   6 R  217  GLN TYR ALA ASN ASN PRO ARG VAL VAL PHE ASN LEU ASN          
SEQRES   7 R  217  THR TYR LYS THR LYS GLU GLU MET ILE VAL ALA THR SER          
SEQRES   8 R  217  GLN THR SER GLN TYR GLY GLY ASP LEU THR ASN THR PHE          
SEQRES   9 R  217  GLY ALA ILE GLN TYR ALA ARG LYS TYR ALA TYR SER ALA          
SEQRES  10 R  217  ALA SER GLY GLY ARG ARG SER ALA THR LYS VAL MET VAL          
SEQRES  11 R  217  VAL VAL THR ASP GLY GLU SER HIS ASP GLY SER MET LEU          
SEQRES  12 R  217  LYS ALA VAL ILE ASP GLN CYS ASN HIS ASP ASN ILE LEU          
SEQRES  13 R  217  ARG PHE GLY ILE ALA VAL LEU GLY TYR LEU ASN ARG ASN          
SEQRES  14 R  217  ALA LEU ASP THR LYS ASN LEU ILE LYS GLU ILE LYS ALA          
SEQRES  15 R  217  ILE ALA SER ILE PRO THR GLU ARG TYR PHE PHE ASN VAL          
SEQRES  16 R  217  SER ASP GLU ALA ALA LEU LEU GLU LYS ALA GLY THR LEU          
SEQRES  17 R  217  GLY GLU GLN ILE PHE SER ILE GLU GLY                          
HET    SO4  A 201       5                                                       
HET    SO4  A 202       5                                                       
HET    SO4  B 201       5                                                       
HET     PR  C 401       1                                                       
HET     NA  C 402       1                                                       
HET     CL  C 403       1                                                       
HET    SO4  D 201       5                                                       
HET    NH4  D 202       1                                                       
HET    SO4  E 201       5                                                       
HET     CL  E 202       1                                                       
HET    SO4  E 203       5                                                       
HET     PR  F 401       1                                                       
HET     NA  F 402       1                                                       
HET     CL  G 201       1                                                       
HET    SO4  G 202       5                                                       
HET     CL  H 201       1                                                       
HET    SO4  H 202       5                                                       
HET     PR  I 401       1                                                       
HET     NA  I 402       1                                                       
HET    SO4  J 201       5                                                       
HET     CL  J 202       1                                                       
HET     CL  K 201       1                                                       
HET    SO4  K 202       5                                                       
HET     PR  L 401       1                                                       
HET     NA  L 402       1                                                       
HET     CL  L 403       1                                                       
HET     CL  M 201       1                                                       
HET    SO4  N 201       5                                                       
HET     PR  O 401       1                                                       
HET     NA  O 402       1                                                       
HET    SO4  O 403       5                                                       
HET    SO4  Q 201       5                                                       
HET    SO4  Q 202       5                                                       
HET     PR  R 401       1                                                       
HET    SO4  R 402       5                                                       
HET     CL  R 403       1                                                       
HET     NA  R 404       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      PR PRASEODYMIUM ION                                                 
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NH4 AMMONIUM ION                                                     
FORMUL  19  SO4    15(O4 S 2-)                                                  
FORMUL  22   PR    6(PR 3+)                                                     
FORMUL  23   NA    6(NA 1+)                                                     
FORMUL  24   CL    9(CL 1-)                                                     
FORMUL  26  NH4    H4 N 1+                                                      
FORMUL  56  HOH   *7(H2 O)                                                      
HELIX    1 AA1 THR A   24  GLN A   35  1                                  12    
HELIX    2 AA2 SER A   46  ILE A   61  1                                  16    
HELIX    3 AA3 ARG A  109  GLY A  112  5                                   4    
HELIX    4 AA4 THR B   21  ALA B   31  1                                  11    
HELIX    5 AA5 SER B   43  LEU B   58  1                                  16    
HELIX    6 AA6 PRO C  187  GLY C  201  1                                  15    
HELIX    7 AA7 THR C  231  SER C  240  1                                  10    
HELIX    8 AA8 ASN C  251  ALA C  263  1                                  13    
HELIX    9 AA9 ASP C  288  SER C  290  5                                   3    
HELIX   10 AB1 MET C  291  ASP C  302  1                                  12    
HELIX   11 AB2 LEU C  312  ASN C  318  1                                   7    
HELIX   12 AB3 THR C  322  ALA C  333  1                                  12    
HELIX   13 AB4 PRO C  336  TYR C  340  1                                   5    
HELIX   14 AB5 ASP C  346  GLU C  352  5                                   7    
HELIX   15 AB6 LYS C  353  ILE C  361  1                                   9    
HELIX   16 AB7 THR D   24  GLU D   34  1                                  11    
HELIX   17 AB8 SER D   46  ILE D   61  1                                  16    
HELIX   18 AB9 ARG D  109  GLY D  112  5                                   4    
HELIX   19 AC1 THR E   21  ALA E   31  1                                  11    
HELIX   20 AC2 SER E   43  LEU E   58  1                                  16    
HELIX   21 AC3 PRO F  187  GLY F  201  1                                  15    
HELIX   22 AC4 THR F  231  GLN F  241  1                                  11    
HELIX   23 AC5 ASN F  251  ALA F  263  1                                  13    
HELIX   24 AC6 ASP F  288  SER F  290  5                                   3    
HELIX   25 AC7 MET F  291  ASP F  302  1                                  12    
HELIX   26 AC8 LEU F  312  ASN F  318  1                                   7    
HELIX   27 AC9 THR F  322  ALA F  333  1                                  12    
HELIX   28 AD1 PRO F  336  TYR F  340  1                                   5    
HELIX   29 AD2 GLU F  347  GLU F  352  5                                   6    
HELIX   30 AD3 LYS F  353  ILE F  361  1                                   9    
HELIX   31 AD4 THR G   24  GLU G   34  1                                  11    
HELIX   32 AD5 SER G   46  ILE G   61  1                                  16    
HELIX   33 AD6 ARG G  109  GLY G  112  5                                   4    
HELIX   34 AD7 THR H   21  ALA H   31  1                                  11    
HELIX   35 AD8 SER H   43  LEU H   58  1                                  16    
HELIX   36 AD9 PRO I  187  GLY I  201  1                                  15    
HELIX   37 AE1 THR I  231  GLN I  241  1                                  11    
HELIX   38 AE2 ASN I  251  ALA I  263  1                                  13    
HELIX   39 AE3 ASP I  288  SER I  290  5                                   3    
HELIX   40 AE4 MET I  291  ASP I  302  1                                  12    
HELIX   41 AE5 LEU I  312  ARG I  317  1                                   6    
HELIX   42 AE6 THR I  322  ALA I  333  1                                  12    
HELIX   43 AE7 PRO I  336  TYR I  340  1                                   5    
HELIX   44 AE8 GLU I  347  GLU I  352  5                                   6    
HELIX   45 AE9 LYS I  353  ILE I  361  1                                   9    
HELIX   46 AF1 THR J   24  GLU J   34  1                                  11    
HELIX   47 AF2 SER J   46  ILE J   61  1                                  16    
HELIX   48 AF3 ARG J  109  GLY J  112  5                                   4    
HELIX   49 AF4 THR K   21  ALA K   31  1                                  11    
HELIX   50 AF5 SER K   43  GLN K   56  1                                  14    
HELIX   51 AF6 PRO L  187  GLY L  201  1                                  15    
HELIX   52 AF7 THR L  231  SER L  240  1                                  10    
HELIX   53 AF8 ASN L  251  ALA L  263  1                                  13    
HELIX   54 AF9 ASP L  288  SER L  290  5                                   3    
HELIX   55 AG1 MET L  291  ASP L  302  1                                  12    
HELIX   56 AG2 LEU L  312  ASN L  318  1                                   7    
HELIX   57 AG3 THR L  322  ALA L  333  1                                  12    
HELIX   58 AG4 PRO L  336  TYR L  340  1                                   5    
HELIX   59 AG5 ASP L  346  GLU L  352  5                                   7    
HELIX   60 AG6 LYS L  353  ILE L  361  1                                   9    
HELIX   61 AG7 THR M   24  GLN M   35  1                                  12    
HELIX   62 AG8 SER M   46  ILE M   61  1                                  16    
HELIX   63 AG9 TRP M  110  GLY M  112  5                                   3    
HELIX   64 AH1 THR N   21  ALA N   31  1                                  11    
HELIX   65 AH2 SER N   43  GLN N   56  1                                  14    
HELIX   66 AH3 TRP O  188  GLY O  201  1                                  14    
HELIX   67 AH4 THR O  231  SER O  240  1                                  10    
HELIX   68 AH5 ASN O  251  ALA O  263  1                                  13    
HELIX   69 AH6 ASP O  288  SER O  290  5                                   3    
HELIX   70 AH7 MET O  291  ASP O  302  1                                  12    
HELIX   71 AH8 LEU O  312  ASN O  318  1                                   7    
HELIX   72 AH9 THR O  322  ALA O  333  1                                  12    
HELIX   73 AI1 PRO O  336  TYR O  340  1                                   5    
HELIX   74 AI2 ASP O  346  ALA O  349  5                                   4    
HELIX   75 AI3 LEU O  350  ILE O  361  1                                  12    
HELIX   76 AI4 THR P   24  GLU P   34  1                                  11    
HELIX   77 AI5 SER P   46  ILE P   61  1                                  16    
HELIX   78 AI6 TRP P  110  GLY P  112  5                                   3    
HELIX   79 AI7 THR Q   21  ALA Q   31  1                                  11    
HELIX   80 AI8 SER Q   43  GLN Q   56  1                                  14    
HELIX   81 AI9 TRP R  188  LEU R  202  1                                  15    
HELIX   82 AJ1 THR R  231  SER R  240  1                                  10    
HELIX   83 AJ2 ASN R  251  ALA R  263  1                                  13    
HELIX   84 AJ3 ASP R  288  SER R  290  5                                   3    
HELIX   85 AJ4 MET R  291  ASP R  302  1                                  12    
HELIX   86 AJ5 LEU R  312  ASN R  318  1                                   7    
HELIX   87 AJ6 THR R  322  ALA R  333  1                                  12    
HELIX   88 AJ7 PRO R  336  TYR R  340  1                                   5    
HELIX   89 AJ8 ASP R  346  ALA R  349  5                                   4    
HELIX   90 AJ9 LEU R  350  ILE R  361  1                                  12    
SHEET    1 AA1 4 SER A   9  TYR A  11  0                                        
SHEET    2 AA1 4 HIS A  14  LYS A  23 -1  O  HIS A  14   N  TYR A  11           
SHEET    3 AA1 4 ASN A 125  PRO A 132 -1  O  PHE A 131   N  CYS A  15           
SHEET    4 AA1 4 HIS A  40  LEU A  41 -1  N  HIS A  40   O  LYS A 130           
SHEET    1 AA2 4 TRP A 116  TYR A 118  0                                        
SHEET    2 AA2 4 CYS A 104  LEU A 107 -1  N  GLY A 106   O  ASP A 117           
SHEET    3 AA2 4 TRP A  69  ARG A  73 -1  N  LEU A  72   O  GLN A 105           
SHEET    4 AA2 4 GLU B  77  TRP B  78 -1  O  GLU B  77   N  ARG A  73           
SHEET    1 AA3 4 SER B   6  TYR B   8  0                                        
SHEET    2 AA3 4 TYR B  11  LYS B  20 -1  O  TYR B  13   N  SER B   6           
SHEET    3 AA3 4 VAL B 116  LYS B 121 -1  O  VAL B 116   N  LYS B  20           
SHEET    4 AA3 4 ARG B  37  LEU B  38 -1  N  ARG B  37   O  LYS B 121           
SHEET    1 AA4 6 SER B   6  TYR B   8  0                                        
SHEET    2 AA4 6 TYR B  11  LYS B  20 -1  O  TYR B  13   N  SER B   6           
SHEET    3 AA4 6 VAL B 116  LYS B 121 -1  O  VAL B 116   N  LYS B  20           
SHEET    4 AA4 6 SER B  62  ASN B  68  1  N  TRP B  64   O  SER B 117           
SHEET    5 AA4 6 TYR B  94  LYS B 101 -1  O  ALA B  96   N  LEU B  65           
SHEET    6 AA4 6 ARG B 104  GLY B 111 -1  O  ARG B 104   N  LYS B 101           
SHEET    1 AA5 6 PRO C 220  PHE C 224  0                                        
SHEET    2 AA5 6 THR C 209  TYR C 216 -1  N  LEU C 213   O  VAL C 223           
SHEET    3 AA5 6 ILE C 173  ASP C 180  1  N  VAL C 177   O  ILE C 214           
SHEET    4 AA5 6 VAL C 277  THR C 282  1  O  VAL C 281   N  ASP C 180           
SHEET    5 AA5 6 LEU C 305  VAL C 311  1  O  PHE C 307   N  VAL C 280           
SHEET    6 AA5 6 PHE C 341  VAL C 344  1  O  VAL C 344   N  ALA C 310           
SHEET    1 AA6 4 SER D   9  TYR D  11  0                                        
SHEET    2 AA6 4 HIS D  14  LYS D  23 -1  O  TYR D  16   N  SER D   9           
SHEET    3 AA6 4 ASN D 125  PHE D 131 -1  O  PHE D 131   N  CYS D  15           
SHEET    4 AA6 4 HIS D  40  LEU D  41 -1  N  HIS D  40   O  LYS D 130           
SHEET    1 AA7 3 TRP D  69  ARG D  73  0                                        
SHEET    2 AA7 3 CYS D 104  LEU D 107 -1  O  GLN D 105   N  LEU D  72           
SHEET    3 AA7 3 TRP D 116  SER D 119 -1  O  ASP D 117   N  GLY D 106           
SHEET    1 AA8 2 SER E   6  TYR E   8  0                                        
SHEET    2 AA8 2 TYR E  11  TYR E  13 -1  O  TYR E  13   N  SER E   6           
SHEET    1 AA9 2 ARG E  37  LEU E  38  0                                        
SHEET    2 AA9 2 CYS E 120  LYS E 121 -1  O  LYS E 121   N  ARG E  37           
SHEET    1 AB1 3 SER E  62  ASN E  68  0                                        
SHEET    2 AB1 3 TYR E  94  VAL E 100 -1  O  MET E  98   N  MET E  63           
SHEET    3 AB1 3 ILE E 105  GLY E 111 -1  O  ARG E 110   N  CYS E  95           
SHEET    1 AB2 6 PRO F 220  PHE F 224  0                                        
SHEET    2 AB2 6 THR F 209  TYR F 216 -1  N  LEU F 213   O  PHE F 224           
SHEET    3 AB2 6 ILE F 173  ASP F 180  1  N  VAL F 177   O  ILE F 214           
SHEET    4 AB2 6 THR F 275  THR F 282  1  O  VAL F 281   N  ASP F 180           
SHEET    5 AB2 6 LEU F 305  VAL F 311  1  O  PHE F 307   N  VAL F 280           
SHEET    6 AB2 6 PHE F 341  VAL F 344  1  O  PHE F 342   N  GLY F 308           
SHEET    1 AB3 4 SER G   9  TYR G  11  0                                        
SHEET    2 AB3 4 HIS G  14  LYS G  23 -1  O  TYR G  16   N  SER G   9           
SHEET    3 AB3 4 ASN G 125  PRO G 132 -1  O  PHE G 131   N  CYS G  15           
SHEET    4 AB3 4 HIS G  40  LEU G  41 -1  N  HIS G  40   O  LYS G 130           
SHEET    1 AB4 4 TRP G 116  SER G 119  0                                        
SHEET    2 AB4 4 CYS G 104  LEU G 107 -1  N  GLY G 106   O  ASP G 117           
SHEET    3 AB4 4 TRP G  69  ASP G  74 -1  N  LEU G  72   O  GLN G 105           
SHEET    4 AB4 4 TRP H  76  TRP H  78 -1  O  GLU H  77   N  ARG G  73           
SHEET    1 AB5 4 SER H   6  TYR H   8  0                                        
SHEET    2 AB5 4 TYR H  11  ARG H  14 -1  O  TYR H  13   N  SER H   6           
SHEET    3 AB5 4 CYS H 120  LYS H 121 -1  O  CYS H 120   N  ARG H  14           
SHEET    4 AB5 4 ARG H  37  LEU H  38 -1  N  ARG H  37   O  LYS H 121           
SHEET    1 AB6 3 SER H  62  ASN H  68  0                                        
SHEET    2 AB6 3 TYR H  94  VAL H 100 -1  O  MET H  98   N  MET H  63           
SHEET    3 AB6 3 ILE H 105  GLY H 111 -1  O  PHE H 106   N  VAL H  99           
SHEET    1 AB7 6 PRO I 220  PHE I 224  0                                        
SHEET    2 AB7 6 THR I 209  TYR I 216 -1  N  LEU I 213   O  VAL I 223           
SHEET    3 AB7 6 ILE I 173  ASP I 180  1  N  VAL I 177   O  ILE I 214           
SHEET    4 AB7 6 VAL I 277  THR I 282  1  O  VAL I 281   N  ASP I 180           
SHEET    5 AB7 6 LEU I 305  VAL I 311  1  O  PHE I 307   N  VAL I 280           
SHEET    6 AB7 6 PHE I 341  VAL I 344  1  O  PHE I 342   N  GLY I 308           
SHEET    1 AB8 4 SER J   9  TYR J  11  0                                        
SHEET    2 AB8 4 HIS J  14  LYS J  23 -1  O  HIS J  14   N  TYR J  11           
SHEET    3 AB8 4 ASN J 125  PHE J 131 -1  O  PHE J 131   N  CYS J  15           
SHEET    4 AB8 4 HIS J  40  LEU J  41 -1  N  HIS J  40   O  LYS J 130           
SHEET    1 AB9 4 TRP J 116  SER J 119  0                                        
SHEET    2 AB9 4 CYS J 104  LEU J 107 -1  N  CYS J 104   O  SER J 119           
SHEET    3 AB9 4 TRP J  69  ARG J  73 -1  N  LEU J  72   O  GLN J 105           
SHEET    4 AB9 4 GLU K  77  TRP K  78 -1  O  GLU K  77   N  ARG J  73           
SHEET    1 AC1 4 SER K   6  TYR K   8  0                                        
SHEET    2 AC1 4 TYR K  11  LYS K  20 -1  O  TYR K  13   N  SER K   6           
SHEET    3 AC1 4 VAL K 116  LYS K 121 -1  O  VAL K 116   N  LYS K  20           
SHEET    4 AC1 4 ARG K  37  LEU K  38 -1  N  ARG K  37   O  LYS K 121           
SHEET    1 AC2 6 SER K   6  TYR K   8  0                                        
SHEET    2 AC2 6 TYR K  11  LYS K  20 -1  O  TYR K  13   N  SER K   6           
SHEET    3 AC2 6 VAL K 116  LYS K 121 -1  O  VAL K 116   N  LYS K  20           
SHEET    4 AC2 6 SER K  62  ASN K  68  1  N  TRP K  64   O  SER K 117           
SHEET    5 AC2 6 TYR K  94  LYS K 101 -1  O  MET K  98   N  MET K  63           
SHEET    6 AC2 6 ARG K 104  GLY K 111 -1  O  ARG K 104   N  LYS K 101           
SHEET    1 AC3 6 PRO L 220  PHE L 224  0                                        
SHEET    2 AC3 6 THR L 209  TYR L 216 -1  N  LEU L 213   O  VAL L 223           
SHEET    3 AC3 6 ILE L 173  ASP L 180  1  N  VAL L 177   O  ILE L 214           
SHEET    4 AC3 6 THR L 275  THR L 282  1  O  VAL L 279   N  VAL L 178           
SHEET    5 AC3 6 LEU L 305  VAL L 311  1  O  PHE L 307   N  VAL L 280           
SHEET    6 AC3 6 PHE L 341  VAL L 344  1  O  VAL L 344   N  ALA L 310           
SHEET    1 AC4 4 SER M   9  TYR M  11  0                                        
SHEET    2 AC4 4 HIS M  14  LYS M  23 -1  O  HIS M  14   N  TYR M  11           
SHEET    3 AC4 4 ASN M 125  PRO M 132 -1  O  ASN M 125   N  LYS M  23           
SHEET    4 AC4 4 HIS M  40  LEU M  41 -1  N  HIS M  40   O  LYS M 130           
SHEET    1 AC5 4 TRP M 116  SER M 119  0                                        
SHEET    2 AC5 4 CYS M 104  ALA M 108 -1  N  CYS M 104   O  SER M 119           
SHEET    3 AC5 4 TYR M  67  ASP M  74 -1  N  VAL M  68   O  LEU M 107           
SHEET    4 AC5 4 TRP N  76  GLU N  77 -1  O  GLU N  77   N  ARG M  73           
SHEET    1 AC6 4 SER N   6  TYR N   8  0                                        
SHEET    2 AC6 4 TYR N  11  ARG N  14 -1  O  TYR N  13   N  SER N   6           
SHEET    3 AC6 4 CYS N 120  LYS N 121 -1  O  CYS N 120   N  ARG N  14           
SHEET    4 AC6 4 ARG N  37  LEU N  38 -1  N  ARG N  37   O  LYS N 121           
SHEET    1 AC7 3 SER N  62  ASN N  68  0                                        
SHEET    2 AC7 3 TYR N  94  VAL N 100 -1  O  ALA N  96   N  LEU N  67           
SHEET    3 AC7 3 ILE N 105  TRP N 107 -1  O  PHE N 106   N  VAL N  99           
SHEET    1 AC8 3 SER N  62  ASN N  68  0                                        
SHEET    2 AC8 3 TYR N  94  VAL N 100 -1  O  ALA N  96   N  LEU N  67           
SHEET    3 AC8 3 ARG N 110  GLY N 111 -1  O  ARG N 110   N  CYS N  95           
SHEET    1 AC9 6 PRO O 220  PHE O 224  0                                        
SHEET    2 AC9 6 GLN O 210  TYR O 216 -1  N  LEU O 213   O  PHE O 224           
SHEET    3 AC9 6 ILE O 173  ASP O 180  1  N  VAL O 177   O  ILE O 214           
SHEET    4 AC9 6 THR O 275  THR O 282  1  O  VAL O 281   N  ASP O 180           
SHEET    5 AC9 6 LEU O 305  VAL O 311  1  O  PHE O 307   N  VAL O 280           
SHEET    6 AC9 6 PHE O 341  VAL O 344  1  O  PHE O 342   N  GLY O 308           
SHEET    1 AD1 4 SER P   9  TYR P  11  0                                        
SHEET    2 AD1 4 HIS P  14  LYS P  23 -1  O  HIS P  14   N  TYR P  11           
SHEET    3 AD1 4 ASN P 125  PRO P 132 -1  O  ASN P 125   N  LYS P  23           
SHEET    4 AD1 4 HIS P  40  LEU P  41 -1  N  HIS P  40   O  LYS P 130           
SHEET    1 AD2 4 TRP P 116  SER P 119  0                                        
SHEET    2 AD2 4 CYS P 104  ALA P 108 -1  N  CYS P 104   O  SER P 119           
SHEET    3 AD2 4 TYR P  67  ASP P  74 -1  N  VAL P  68   O  LEU P 107           
SHEET    4 AD2 4 TRP Q  76  TRP Q  78 -1  O  GLU Q  77   N  ARG P  73           
SHEET    1 AD3 4 SER Q   6  TYR Q   8  0                                        
SHEET    2 AD3 4 TYR Q  11  LYS Q  20 -1  O  TYR Q  13   N  SER Q   6           
SHEET    3 AD3 4 VAL Q 116  LYS Q 121 -1  O  VAL Q 116   N  LYS Q  20           
SHEET    4 AD3 4 ARG Q  37  LEU Q  38 -1  N  ARG Q  37   O  LYS Q 121           
SHEET    1 AD4 6 SER Q   6  TYR Q   8  0                                        
SHEET    2 AD4 6 TYR Q  11  LYS Q  20 -1  O  TYR Q  13   N  SER Q   6           
SHEET    3 AD4 6 VAL Q 116  LYS Q 121 -1  O  VAL Q 116   N  LYS Q  20           
SHEET    4 AD4 6 SER Q  62  ASN Q  68  1  N  TRP Q  64   O  SER Q 117           
SHEET    5 AD4 6 TYR Q  94  VAL Q 100 -1  O  ALA Q  96   N  LEU Q  67           
SHEET    6 AD4 6 ILE Q 105  GLY Q 111 -1  O  ARG Q 110   N  CYS Q  95           
SHEET    1 AD5 6 PRO R 220  PHE R 224  0                                        
SHEET    2 AD5 6 GLN R 210  TYR R 216 -1  N  LEU R 213   O  PHE R 224           
SHEET    3 AD5 6 ILE R 173  ASP R 180  1  N  VAL R 177   O  ILE R 214           
SHEET    4 AD5 6 THR R 275  THR R 282  1  O  VAL R 281   N  ASP R 180           
SHEET    5 AD5 6 LEU R 305  VAL R 311  1  O  PHE R 307   N  VAL R 280           
SHEET    6 AD5 6 PHE R 341  VAL R 344  1  O  VAL R 344   N  ALA R 310           
SSBOND   1 CYS A    4    CYS A   15                          1555   1555  2.03  
SSBOND   2 CYS A   32    CYS A  129                          1555   1555  2.02  
SSBOND   3 CYS A   81    CYS B   74                          1555   1555  2.06  
SSBOND   4 CYS A  104    CYS A  121                          1555   1555  2.05  
SSBOND   5 CYS B    1    CYS B   12                          1555   1555  2.04  
SSBOND   6 CYS B   29    CYS B  120                          1555   1555  2.03  
SSBOND   7 CYS B   95    CYS B  112                          1555   1555  2.05  
SSBOND   8 CYS D    4    CYS D   15                          1555   1555  2.03  
SSBOND   9 CYS D   32    CYS D  129                          1555   1555  2.05  
SSBOND  10 CYS D   81    CYS E   74                          1555   1555  2.04  
SSBOND  11 CYS D  104    CYS D  121                          1555   1555  2.00  
SSBOND  12 CYS E    1    CYS E   12                          1555   1555  2.04  
SSBOND  13 CYS E   29    CYS E  120                          1555   1555  2.06  
SSBOND  14 CYS E   95    CYS E  112                          1555   1555  2.05  
SSBOND  15 CYS G    4    CYS G   15                          1555   1555  2.02  
SSBOND  16 CYS G   32    CYS G  129                          1555   1555  2.05  
SSBOND  17 CYS G   81    CYS H   74                          1555   1555  2.03  
SSBOND  18 CYS G  104    CYS G  121                          1555   1555  2.01  
SSBOND  19 CYS H    1    CYS H   12                          1555   1555  2.03  
SSBOND  20 CYS H   29    CYS H  120                          1555   1555  2.07  
SSBOND  21 CYS H   95    CYS H  112                          1555   1555  2.05  
SSBOND  22 CYS J    4    CYS J   15                          1555   1555  2.02  
SSBOND  23 CYS J   32    CYS J  129                          1555   1555  2.01  
SSBOND  24 CYS J   81    CYS K   74                          1555   1555  2.05  
SSBOND  25 CYS J  104    CYS J  121                          1555   1555  2.04  
SSBOND  26 CYS K    1    CYS K   12                          1555   1555  2.03  
SSBOND  27 CYS K   29    CYS K  120                          1555   1555  2.03  
SSBOND  28 CYS K   95    CYS K  112                          1555   1555  2.06  
SSBOND  29 CYS M    4    CYS M   15                          1555   1555  2.04  
SSBOND  30 CYS M   32    CYS M  129                          1555   1555  2.08  
SSBOND  31 CYS M   81    CYS N   74                          1555   1555  2.01  
SSBOND  32 CYS M  104    CYS M  121                          1555   1555  2.01  
SSBOND  33 CYS N    1    CYS N   12                          1555   1555  2.04  
SSBOND  34 CYS N   29    CYS N  120                          1555   1555  2.07  
SSBOND  35 CYS N   95    CYS N  112                          1555   1555  2.03  
SSBOND  36 CYS P    4    CYS P   15                          1555   1555  2.03  
SSBOND  37 CYS P   32    CYS P  129                          1555   1555  2.08  
SSBOND  38 CYS P   81    CYS Q   74                          1555   1555  2.02  
SSBOND  39 CYS P  104    CYS P  121                          1555   1555  2.01  
SSBOND  40 CYS Q    1    CYS Q   12                          1555   1555  2.04  
SSBOND  41 CYS Q   29    CYS Q  120                          1555   1555  2.07  
SSBOND  42 CYS Q   95    CYS Q  112                          1555   1555  2.03  
LINK         OG  SER C 182                PR    PR C 401     1555   1555  2.83  
LINK         OG  SER C 184                PR    PR C 401     1555   1555  2.19  
LINK         OD1 ASP C 283                PR    PR C 401     1555   1555  2.70  
LINK         OG  SER F 182                PR    PR F 401     1555   1555  2.54  
LINK         OG  SER F 184                NA    NA F 402     1555   1555  2.62  
LINK         OG  SER F 184                PR    PR F 401     1555   1555  2.67  
LINK         OD1 ASP F 283                PR    PR F 401     1555   1555  2.67  
LINK         OG  SER I 182                PR    PR I 401     1555   1555  2.38  
LINK         OG  SER I 184                PR    PR I 401     1555   1555  2.73  
LINK         OG  SER I 184                NA    NA I 402     1555   1555  2.58  
LINK         OD1 ASP I 283                PR    PR I 401     1555   1555  2.75  
LINK         OG  SER L 182                PR    PR L 401     1555   1555  2.88  
LINK         OG  SER L 184                PR    PR L 401     1555   1555  2.27  
LINK         OD1 ASP L 283                PR    PR L 401     1555   1555  2.73  
LINK         OG  SER O 182                PR    PR O 401     1555   1555  2.99  
LINK         OG  SER O 184                PR    PR O 401     1555   1555  2.10  
LINK         OD1 ASP O 283                PR    PR O 401     1555   1555  2.73  
LINK         OG  SER R 182                PR    PR R 401     1555   1555  2.95  
LINK         OD1 ASP R 283                PR    PR R 401     1555   1555  2.80  
LINK         O3  SO4 B 201                NA    NA C 402     1555   1555  2.37  
LINK         O3  SO4 E 203                NA    NA F 402     1555   1555  2.85  
LINK         O3  SO4 H 202                NA    NA I 402     1555   1555  2.86  
LINK         O3  SO4 K 202                NA    NA L 402     1555   1555  2.52  
LINK         O4  SO4 N 201                NA    NA O 402     1555   1555  2.05  
LINK         O3  SO4 Q 202                NA    NA R 404     1555   1555  2.22  
CISPEP   1 TYR C  186    PRO C  187          0       -13.21                     
CISPEP   2 ILE C  335    PRO C  336          0        -3.96                     
CISPEP   3 TYR F  186    PRO F  187          0       -10.97                     
CISPEP   4 ILE F  335    PRO F  336          0         1.53                     
CISPEP   5 TYR I  186    PRO I  187          0       -10.97                     
CISPEP   6 ILE I  335    PRO I  336          0         3.00                     
CISPEP   7 TYR L  186    PRO L  187          0       -11.43                     
CISPEP   8 ILE L  335    PRO L  336          0        -4.08                     
CISPEP   9 TYR O  186    PRO O  187          0       -18.60                     
CISPEP  10 ILE O  335    PRO O  336          0        -5.94                     
CISPEP  11 TYR R  186    PRO R  187          0       -16.52                     
CISPEP  12 ILE R  335    PRO R  336          0        -5.77                     
SITE     1 AC1  3 PHE A  19  ASN A  20  GLU A  21                               
SITE     1 AC2  2 ARG A  73  ARG A  75                                          
SITE     1 AC3  6 ARG B  92  LYS B 114  ASP C 248  THR C 250                    
SITE     2 AC3  6  PR C 401   NA C 402                                          
SITE     1 AC4  4 SO4 B 201  SER C 182  SER C 184  ASP C 283                    
SITE     1 AC5  4 SO4 B 201  ASN C 183  SER C 184  GLY C 247                    
SITE     1 AC6  1 ARG C 339                                                     
SITE     1 AC7  4 PHE D  19  ASN D  20  GLU D  21  NH4 D 202                    
SITE     1 AC8  4 GLN D  17  ALA D  18  PHE D  19  SO4 D 201                    
SITE     1 AC9  2 LYS E 101  ARG E 104                                          
SITE     1 AD1  1 LYS E  59                                                     
SITE     1 AD2  7 ARG E 110  LYS E 114  SER F 184  THR F 250                    
SITE     2 AD2  7 TYR F 314   PR F 401   NA F 402                               
SITE     1 AD3  5 SO4 E 203  ASP F 180  SER F 182  SER F 184                    
SITE     2 AD3  5 ASP F 283                                                     
SITE     1 AD4  2 SO4 E 203  SER F 184                                          
SITE     1 AD5  2 ARG C 260  GLY G   7                                          
SITE     1 AD6  3 PHE G  19  ASN G  20  GLU G  21                               
SITE     1 AD7  1 LYS H  59                                                     
SITE     1 AD8  6 ARG H 110  LYS H 114  SER I 184  THR I 250                    
SITE     2 AD8  6 TYR I 314   NA I 402                                          
SITE     1 AD9  4 ASP I 180  SER I 182  SER I 184  ASP I 283                    
SITE     1 AE1  2 SO4 H 202  SER I 184                                          
SITE     1 AE2  3 PHE J  19  ASN J  20  GLU J  21                               
SITE     1 AE3  2 ARG J  73  ARG J  75                                          
SITE     1 AE4  5 ARG K  92  LYS K 114  ASP L 248  THR L 250                    
SITE     2 AE4  5  NA L 402                                                     
SITE     1 AE5  3 SER L 182  SER L 184  ASP L 283                               
SITE     1 AE6  4 SO4 K 202  ASN L 183  SER L 184  GLY L 247                    
SITE     1 AE7  2 GLN M 102  ARG N  91                                          
SITE     1 AE8  5 ARG N  92  LYS N 114  ASP O 248  THR O 250                    
SITE     2 AE8  5  NA O 402                                                     
SITE     1 AE9  3 SER O 182  SER O 184  ASP O 283                               
SITE     1 AF1  2 SO4 N 201  SER O 184                                          
SITE     1 AF2  4 GLN O 257  ARG O 260  LYS O 261  GLN O 298                    
SITE     1 AF3  2 TYR Q   8  ASN Q   9                                          
SITE     1 AF4  5 ARG Q  92  LYS Q 114  ASP R 248  THR R 250                    
SITE     2 AF4  5  NA R 404                                                     
SITE     1 AF5  3 SER R 182  SER R 184  ASP R 283                               
SITE     1 AF6  4 GLN R 257  ARG R 260  LYS R 261  GLN R 298                    
SITE     1 AF7  2 SO4 Q 202  GLY R 247                                          
CRYST1  132.351  132.351  254.244  90.00  90.00  90.00 P 41         24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007556  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007556  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003933        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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